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1rjx

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[[Image:1rjx.jpg|left|200px]]
[[Image:1rjx.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1rjx |SIZE=350|CAPTION= <scene name='initialview01'>1rjx</scene>, resolution 2.3&Aring;
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The line below this paragraph, containing "STRUCTURE_1rjx", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Plasmin Plasmin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.7 3.4.21.7] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= PLG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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-->
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|DOMAIN=
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{{STRUCTURE_1rjx| PDB=1rjx | SCENE= }}
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|RELATEDENTRY=[[1ddj|1DDJ]], [[1qrz|1QRZ]], [[1l4d|1L4D]], [[1l4z|1L4Z]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rjx OCA], [http://www.ebi.ac.uk/pdbsum/1rjx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rjx RCSB]</span>
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}}
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'''Human PLASMINOGEN CATALYTIC DOMAIN, K698M MUTANT'''
'''Human PLASMINOGEN CATALYTIC DOMAIN, K698M MUTANT'''
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[[Category: Zhai, P.]]
[[Category: Zhai, P.]]
[[Category: Zhang, X C.]]
[[Category: Zhang, X C.]]
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[[Category: microplasminogen]]
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[[Category: Microplasminogen]]
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[[Category: plasminogen activation]]
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[[Category: Plasminogen activation]]
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[[Category: streptokinase]]
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[[Category: Streptokinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:35:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:29:13 2008''
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Revision as of 04:35, 3 May 2008

Template:STRUCTURE 1rjx

Human PLASMINOGEN CATALYTIC DOMAIN, K698M MUTANT


Contents

Overview

Streptokinase (SK) is a human plasminogen (Pg) activator secreted by streptococci. The activation mechanism of SK differs from that of physiological Pg activators in that SK is not a protease and cannot proteolytically activate Pg. Instead, it forms a tight complex with Pg that proteolytically activates other Pg molecules. The residue Lys-698 of human Pg was hypothesized to participate in triggering activation in the SK-Pg complex. Here, we report a study of the Lys-698 to Met substitution in the catalytic domain of Pg (microPg) containing the proteolytic activation-resistant background (R561A). While it remains competent in forming a complex with SK, maintaining a comparable equilibration dissociation constant (K(D)), the recombinant protein shows a nearly 60-fold reduction in amidolytic activity relative to its R561A background when mixed with native SK. A 2.3 A crystal structure of this mutant microPg confirmed the correct folding of this recombinant protein. Combined with other biochemical data, these results support the premise that Lys-698 of human Pg plays a functional role in the so-called N-terminal insertion activation mechanism by SK.

Disease

Known disease associated with this structure: Conjunctivitis, ligneous OMIM:[173350], Plasminogen Tochigi disease OMIM:[173350], Plasminogen deficiency, types I and II OMIM:[173350], Thrombophilia, dysplasminogenemic OMIM:[173350]

About this Structure

1RJX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Characterization of Lys-698-to-Met substitution in human plasminogen catalytic domain., Terzyan S, Wakeham N, Zhai P, Rodgers K, Zhang XC, Proteins. 2004 Aug 1;56(2):277-84. PMID:15211511 Page seeded by OCA on Sat May 3 07:35:18 2008

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